4XEN

High pressure protein crystallography of hen egg white lysozyme in complex with Tetra-N-acetylchitotetraose at 920 MPa

4XEN の概要

• エントリーDOI: 10.2210/pdb4xen/pdb
• 関連するPDBエントリー: 4wld 4wlt 4wlx 4wly 4wm1 4wm2 4wm3 4wm4 4wm5 4wm6
• 分子名称: Lysozyme C, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15326.75

構造登録者

Yamada, H.,Watanabe, N.,Nagae, T. (登録日: 2014-12-24, 公開日: 2015-04-08, 最終更新日: 2024-11-06)

主引用文献

Yamada, H.,Nagae, T.,Watanabe, N.
High-pressure protein crystallography of hen egg-white lysozyme
Acta Crystallogr.,Sect.D, 71:742-753, 2015

PubMed Abstract: Crystal structures of hen egg-white lysozyme (HEWL) determined under pressures ranging from ambient pressure to 950 MPa are presented. From 0.1 to 710 MPa, the molecular and internal cavity volumes are monotonically compressed. However, from 710 to 890 MPa the internal cavity volume remains almost constant. Moreover, as the pressure increases to 950 MPa, the tetragonal crystal of HEWL undergoes a phase transition from P43212 to P43. Under high pressure, the crystal structure of the enzyme undergoes several local and global changes accompanied by changes in hydration structure. For example, water molecules penetrate into an internal cavity neighbouring the active site and induce an alternate conformation of one of the catalytic residues, Glu35. These phenomena have not been detected by conventional X-ray crystal structure analysis and might play an important role in the catalytic activity of HEWL.

PubMed: 25849385
DOI: 10.1107/S1399004715000292

実験手法

X-RAY DIFFRACTION (1.55 Å)